Investigative Ophthalmology & Visual Science Cover Image for Volume 65, Issue 7
June 2024
Volume 65, Issue 7
Open Access
ARVO Annual Meeting Abstract  |   June 2024
Mechanisms of Peripheral Membrane Protein distribution in the Photoreceptor Outer Segment
Author Affiliations & Notes
  • Faizan Zaidi
    Ophthalmology and Visual Sciences, SUNY Upstate Medical University, Syracuse, New York, United States
  • Peter D Calvert
    Ophthalmology and Visual Sciences, SUNY Upstate Medical University, Syracuse, New York, United States
  • Footnotes
    Commercial Relationships   Faizan Zaidi None; Peter Calvert None
  • Footnotes
    Support  NIH Grant R01EY0182421; R01EY028303
Investigative Ophthalmology & Visual Science June 2024, Vol.65, 4768. doi:
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      Faizan Zaidi, Peter D Calvert; Mechanisms of Peripheral Membrane Protein distribution in the Photoreceptor Outer Segment. Invest. Ophthalmol. Vis. Sci. 2024;65(7):4768.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Purpose : The majority of phototransduction proteins are peripheral membrane proteins. We know that they are localized to the photoreceptor outer segment (OS). However, their distribution within the outer segment and along the discs is poorly understood. Our recent publication using peripheral membrane probes shows that there is inhomogeneities in their distributions forming gradients along the outer segment length (Maza et al., 2019). Our preliminary results also show potential inhomogeneities along the disc surfaces as well. Our study aims to understand, mechanistically, how the inhomogeneous distributions are generated.

Methods : Lipidated EGFP probes and probes consisting of EGFP labeled peptides from photoreceptor proteins were expressed transgenically in Xenopus rod photoreceptors. Rods in the explant retina were imaged using two-photon time-resolved fluorescence anisotropy imaging (2P-trFAIM). In this approach, a highly polarized Ti:S laser (λ=820 nm) was used to excite the EGFP labeled molecules in the photoreceptors. The polarization specific emission was recorded by two orthogonally positioned single-photon detectors that were placed after a polarizing beam splitter in the emission path. Time-resolved polarization images of the rods were gathered and analyzed for anisotropy decay-based homoFRET.

Results : Prenylated probes formed a gradient from the base to the tip of the OS while the myristoylated probes were homogenous throughout the OS. Both probes displayed the time-dependent loss of polarization. However, the prenylated, especially farnesylated, probes contained a fast decay phase corresponding to homo-FRET. The anisotropy decay of myristoylated probes was monotonic and slow, corresponding to rotational diffusion. Similar, distribution and FRET differences were seen in the rhodopsin kinase and transducin α peptide probes.

Conclusions : Our results demonstrate that post-translational lipidation plays a key role in OS distribution and enrichment along the disk surface. This suggests the possibility that probes are being partitioned into different membrane nanodomains based on their lipidation properties.

Maza, N. A., Schiesser, W. E., & Calvert, P. D. (2019). An intrinsic compartmentalization code for peripheral membrane proteins in photoreceptor neurons. J Cell Biol, 218(11), 3753-3772.

This abstract was presented at the 2024 ARVO Annual Meeting, held in Seattle, WA, May 5-9, 2024.

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